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AB79247

Recombinant human PPIL1 protein (His tag C-Terminus)

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Recombinant human PPIL1 protein (His tag C-Terminus) is a Human Full Length protein, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, WB, FuncS.

View Alternative Names

CYPL1, CGI-124, UNQ2425/PRO4984, PPIL1, Peptidyl-prolyl cis-trans isomerase-like 1, PPIase, Rotamase PPIL1

2 Images
Western blot - Recombinant human PPIL1 protein (His tag C-Terminus) (AB79247)
  • WB

Unknown

Western blot - Recombinant human PPIL1 protein (His tag C-Terminus) (AB79247)

All lanes:

Anti-PPIL1 antibody (<a href='/en-us/products/unavailable/ppil1-antibody-ab57195'>ab57195</a>) at 1 µg/mL

Lane 1:

Western blot - Recombinant human PPIL1 protein (His tag C-Terminus) (ab79247) at 0.1 µg

Lane 2:

Western blot - Recombinant human PPIL1 protein (His tag C-Terminus) (ab79247) at 0.01 µg

Secondary

All lanes:

Western blot - Goat Anti-Mouse IgG H&L (HRP) preadsorbed (<a href='/en-us/products/secondary-antibodies/goat-mouse-igg-h-l-hrp-preadsorbed-ab97040'>ab97040</a>) at 1/5000 dilution

true

Exposure time: 30s

SDS-PAGE - Recombinant human PPIL1 protein (His tag C-Terminus) (AB79247)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human PPIL1 protein (His tag C-Terminus) (AB79247)

15% SDS-PAGE showing ab79247 at approximately 19kDa (3μg).

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag C-Terminus

Applications

FuncS, WB, SDS-PAGE

applications

Biologically active

Yes

Biological activity

Specific activity is > 700 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1 nmole of suc-AAPF-pNA per minute at 37°C in Tris-Hcl pH8.0 using chymotrypsin.

Accession

Q9Y3C6

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 0.316% Tris HCl

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>ab79247 can be used as a WB positive control in conjunction with <a href='/en-us/products/unavailable/ppil1-antibody-ab57195'>ab57195</a>.</p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MAAIPPDSWQPPNVYLETSMGIIVLELYWKHAPKTCKNFAELARRGYYNGTKFHRIIKDFMIQGGDPTGTGRGGASIYGKQFEDELHPDLKFTGAGILAMANAGPDTNGSQFFVTLAPTQWLDGKHTIFGRVCQGIGMVNRVGMVETNSQDRPVDDVKIIKAYPSGLEHHHHHH","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q9Y3C6","tags":[{"tag":"His","terminus":"C-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

PPIL1 known as Peptidylprolyl Isomerase Like 1 is an enzyme that functions as a peptidyl-prolyl cis-trans isomerase. It facilitates protein folding by catalyzing the isomerization of proline residues in polypeptide chains. PPIL1 carries a mass of approximately 18 kDa. This protein is expressed in various tissues including the brain and immune system indicating its role in diverse cellular processes.
Biological function summary

PPIL1 contributes significantly to cellular activities by facilitating protein conformational modifications. It often operates as part of larger complexes interacting with other proteins to maintain cellular homeostasis. PPIL1 plays a vital role in response to different cellular stress conditions and its activity affects basic cellular functions especially those involving protein assembly and signaling.

Pathways

PPIL1 interacts with several critical signaling pathways influencing protein folding and cellular stress responses. It is notably involved in the protein processing pathway where it modulates the action of related proteins like Cyclophilin A (CYPA). These interactions are essential for maintaining protein homeostasis affecting processes such as cell cycle progression and apoptosis.

Abnormalities in PPIL1 expression or function have been linked to various pathological conditions such as cancer and neurodegenerative diseases. In these diseases PPIL1 may affect tumor growth or neuronal survival by interacting with proteins like p53 which is important in cancer cell apoptosis regulation. These interactions highlight PPIL1's potential as a therapeutic target for drug development and disease treatment strategies.

Specifications

Form

Liquid

Additional notes

ab79247 is purified using conventional chromatography techniques.

General info

Function

Involved in pre-mRNA splicing as component of the spliceosome (PubMed : 11991638, PubMed : 28076346, PubMed : 28502770, PubMed : 33220177). PPIases accelerate the folding of proteins. Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed : 16595688). Catalyzes prolyl peptide bond isomerization in CDC40/PRP17 (PubMed : 33220177). Plays an important role in embryonic brain development; this function is independent of its isomerase activity (PubMed : 33220177).

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIL1 subfamily.

Subcellular localisation

Nucleus

Product protocols

Target data

Involved in pre-mRNA splicing as component of the spliceosome (PubMed : 11991638, PubMed : 28076346, PubMed : 28502770, PubMed : 33220177). PPIases accelerate the folding of proteins. Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed : 16595688). Catalyzes prolyl peptide bond isomerization in CDC40/PRP17 (PubMed : 33220177). Plays an important role in embryonic brain development; this function is independent of its isomerase activity (PubMed : 33220177).
See full target information PPIL1

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